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Related Concept Videos

Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

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Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Related Experiment Video

Updated: Sep 9, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Research progress on NAT10-mediated acetylation in normal development and disease.

Da Qin1, Qing Liu1, Xiaochao Ma1

  • 1Department of Thoracic Surgery II, Organ Transplantation Center, The First Hospital of Jilin University, Changchun, China.

Frontiers in Cell and Developmental Biology
|August 29, 2025
PubMed
Summary

N4-acetylcytidine (ac4C) is an RNA modification impacting RNA stability and translation. NAT10 enzyme-mediated ac4C is crucial in physiological processes and cancer, offering therapeutic potential.

Keywords:
AC4CNAT10RNA modificationcancerepitranscriptomicstherapeutic target

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • N4-acetylcytidine (ac4C) is an evolutionarily conserved RNA modification.
  • This modification is catalyzed by the acetyltransferase NAT10, a dual-function enzyme.
  • ac4C regulates RNA stability, translation, and various post-transcriptional processes.

Purpose of the Study:

  • To review the structural and functional roles of NAT10-mediated acetylation.
  • To explore the involvement of NAT10 in physiological contexts and cancer.
  • To highlight emerging therapeutic opportunities targeting NAT10 and ac4C.

Main Methods:

  • Literature review of structural and functional studies on NAT10.
  • Analysis of NAT10's roles in cell division, differentiation, inflammation, aging, and viral infection.
  • Examination of NAT10's oncogenic mechanisms and interactions with non-coding RNAs.

Main Results:

  • NAT10-mediated acetylation plays significant roles in physiological processes.
  • In cancer, NAT10 drives tumor progression via enhanced mRNA stability, cell cycle regulation, metastasis, and immune evasion.
  • NAT10 also influences ferroptosis, metabolism, p53 activity, and drug resistance.

Conclusions:

  • NAT10-mediated acetylation is a key regulator in both normal physiology and cancer.
  • Targeting NAT10 and ac4C modifications presents promising therapeutic strategies.
  • Future research should address microbiota-mediated ac4C regulation and the tumor immune microenvironment.